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5 results on '"Madugundu, Anil Kumar"'

1. Mass Spectrometric Analysis of Urine from COVID-19 Patients for Detection of SARS-CoV-2 Viral Antigen and to Study Host Response

Author

Chavan, Sandip, primary, Mangalaparthi, Kiran K., additional, Singh, Smrita, additional, Renuse, Santosh, additional, Vanderboom, Patrick M., additional, Madugundu, Anil Kumar, additional, Budhraja, Rohit, additional, McAulay, Kathrine, additional, Grys, Thomas E., additional, Rule, Andrew D., additional, Alexander, Mariam P., additional, O’Horo, John C., additional, Badley, Andrew D., additional, and Pandey, Akhilesh, additional

Published
2021
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3. A draft map of the human proteome

Author

Kim, Minsik, Pinto, Sneha Maria Aria, Getnet, Derese, Nirujogi, Raja Sekhar Ekhar, Manda, Srikanth Srinivas Rinivas, Chaerkady, Raghothama, Madugundu, Anil Kumar, Kelkar, Dhanashree, Isserlin, Ruth, Jain, Shobhit, Thomas, Joji Kurian, Muthusamy, Babylakshmi, Leal-Rojas, Pamela, Kumar, Praveen, Sahasrabuddhe, Nandini, Balakrishnan, Lavanya, Advani, Jayshree, George, Bijesh, Renuse, Santosh, Selvan, Lakshmi Dhevi Nagarajha Nagarajha, Patil, Arun, Nanjappa, Vishalakshi, Radhakrishnan, Aneesha, Prasad, Samarjeet, Subbannayya, Tejaswini, Raju, Rajesh, Kumar, Manish Vijaya, Sreenivasamurthy, Sreelakshmi, Marimuthu, Arivusudar, Sathe, Gajanan, Chavan, Sandip, Datta, Keshava, Subbannayya, Yashwanth, Sahu, Apeksha, Yelamanchi, Soujanya, Jayaram, Savita, Rajagopalan, Pavithra, Sharma, Jyoti, Murthy, Krishna Ramachandra, Syed, Nazia, Goel, Renu, Khan, Aafaqueahmad, Ahmad, Sartaj Akhtar, Dey, Gourav, Mudgal, Keshav, Chatterjee, Aditi, Huang, Taichung, Zhong, Jun, Wu, Xinyan, Shaw, Patrick, Freed, Donald, Zahari, Muhammad Saddiq, Mukherjee, Kanchan Kumar, Shankar, Subramanian Ravi, Mahadevan, Anita, Lam, Henry H N, Mitchell, Christopher, Shankar, Susarla Krishna Rishna, Satishchandra, Parthasarathy, Schroeder, John, Sirdeshmukh, Ravi, Maitra, Anirban, Leach, Steven, Drake, Charles, Halushka, Marc Kenneth, Prasad, Thottethodi Subrahmanya Keshava, Hruban, Ralph, Kerr, Candace, Bader, Gary, Iacobuzio-Donahue, Christine, Gowda, Harsha, Pandey, Akhilesh, Kim, Minsik, Pinto, Sneha Maria Aria, Getnet, Derese, Nirujogi, Raja Sekhar Ekhar, Manda, Srikanth Srinivas Rinivas, Chaerkady, Raghothama, Madugundu, Anil Kumar, Kelkar, Dhanashree, Isserlin, Ruth, Jain, Shobhit, Thomas, Joji Kurian, Muthusamy, Babylakshmi, Leal-Rojas, Pamela, Kumar, Praveen, Sahasrabuddhe, Nandini, Balakrishnan, Lavanya, Advani, Jayshree, George, Bijesh, Renuse, Santosh, Selvan, Lakshmi Dhevi Nagarajha Nagarajha, Patil, Arun, Nanjappa, Vishalakshi, Radhakrishnan, Aneesha, Prasad, Samarjeet, Subbannayya, Tejaswini, Raju, Rajesh, Kumar, Manish Vijaya, Sreenivasamurthy, Sreelakshmi, Marimuthu, Arivusudar, Sathe, Gajanan, Chavan, Sandip, Datta, Keshava, Subbannayya, Yashwanth, Sahu, Apeksha, Yelamanchi, Soujanya, Jayaram, Savita, Rajagopalan, Pavithra, Sharma, Jyoti, Murthy, Krishna Ramachandra, Syed, Nazia, Goel, Renu, Khan, Aafaqueahmad, Ahmad, Sartaj Akhtar, Dey, Gourav, Mudgal, Keshav, Chatterjee, Aditi, Huang, Taichung, Zhong, Jun, Wu, Xinyan, Shaw, Patrick, Freed, Donald, Zahari, Muhammad Saddiq, Mukherjee, Kanchan Kumar, Shankar, Subramanian Ravi, Mahadevan, Anita, Lam, Henry H N, Mitchell, Christopher, Shankar, Susarla Krishna Rishna, Satishchandra, Parthasarathy, Schroeder, John, Sirdeshmukh, Ravi, Maitra, Anirban, Leach, Steven, Drake, Charles, Halushka, Marc Kenneth, Prasad, Thottethodi Subrahmanya Keshava, Hruban, Ralph, Kerr, Candace, Bader, Gary, Iacobuzio-Donahue, Christine, Gowda, Harsha, and Pandey, Akhilesh

Abstract

The availability of human genome sequence has transformed biomedical research over the past decade. However, an equivalent map for the human proteome with direct measurements of proteins and peptides does not exist yet. Here we present a draft map of the human proteome using high-resolution Fourier-transform mass spectrometry. In-depth proteomic profiling of 30 histologically normal human samples, including 17 adult tissues, 7 fetal tissues and 6 purified primary haematopoietic cells, resulted in identification of proteins encoded by 17,294 genes accounting for approximately 84% of the total annotated protein-coding genes in humans. A unique and comprehensive strategy for proteogenomic analysis enabled us to discover a number of novel protein-coding regions, which includes translated pseudogenes, non-coding RNAs and upstream open reading frames. This large human proteome catalogue (available as an interactive web-based resource at http://www.humanproteomemap.org) will complement available human genome and transcriptome data to accelerate biomedical research in health and disease. © 2014 Macmillan Publishers Limited.

Published
2014

4. Multiple Mechanisms Contribute to Lateral Transfer of an Organophosphate Degradation (opd) Island in Sphingobium fuliginis ATCC 27551

Author

Pandeeti, Emmanuel Vijay Paul, primary, Longkumer, Toshisangba, additional, Chakka, Deviprasanna, additional, Muthyala, Venkateswar Reddy, additional, Parthasarathy, Sunil, additional, Madugundu, Anil Kumar, additional, Ghanta, Sujana, additional, Medipally, Srikanth Reddy, additional, Pantula, Surat Chameli, additional, Yekkala, Harshita, additional, and Siddavattam, Dayananda, additional

Published
2012
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5. Multiple mechanisms contribute to lateral transfer of an organophosphate degradation (opd) island in Sphingobium fuliginis ATCC 27551.

Author

Pandeeti EV, Longkumer T, Chakka D, Muthyala VR, Parthasarathy S, Madugundu AK, Ghanta S, Medipally SR, Pantula SC, Yekkala H, and Siddavattam D

Subjects
Attachment Sites, Microbiological, Bacterial Proteins genetics, Bacterial Proteins metabolism, Base Sequence, Cloning, Molecular, Escherichia coli metabolism, Integrases genetics, Integrases metabolism, Molecular Sequence Data, Multigene Family, Organophosphates chemistry, Plasmids genetics, Plasmids metabolism, Recombination, Genetic, Replication Origin genetics, Serine-tRNA Ligase genetics, Gene Transfer, Horizontal, Genes, Bacterial, Organophosphates metabolism, Sphingomonadaceae genetics
Abstract

The complete sequence of pPDL2 (37,317 bp), an indigenous plasmid of Sphingobium fuliginis ATCC 27551 that encodes genes for organophosphate degradation (opd), revealed the existence of a site-specific integrase (int) gene with an attachment site attP, typically seen in integrative mobilizable elements (IME). In agreement with this sequence information, site-specific recombination was observed between pPDL2 and an artificial plasmid having a temperature-sensitive replicon and a cloned attB site at the 3' end of the seryl tRNA gene of Sphingobium japonicum. The opd gene cluster on pPDL2 was found to be part of an active catabolic transposon with mobile elements y4qE and Tn3 at its flanking ends. Besides the previously reported opd cluster, this transposon contains genes coding for protocatechuate dioxygenase and for two transport proteins from the major facilitator family that are predicted to be involved in transport and metabolism of aromatic compounds. A pPDL2 derivative, pPDL2-K, was horizontally transferred into Escherichia coli and Acinetobacter strains, suggesting that the oriT identified in pPDL2 is functional. A well-defined replicative origin (oriV), repA was identified along with a plasmid addiction module relB/relE that would support stable maintenance of pPDL2 in Sphingobium fuliginis ATCC 27551. However, if pPDL2 is laterally transferred into hosts that do not support its replication, the opd cluster appears to integrate into the host chromosome, either through transposition or through site-specific integration. The data presented in this study help to explain the existence of identical opd genes among soil bacteria.

Published
2012
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